Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP.

Abstract:

:Signal recognition particle (SRP), a small ribonucleoprotein required for targeting secretory proteins to the ER, has three known functions: signal recognition, elongation arrest, and translocation promotion. Because SRP is inactivated by the sulfhydryl alkylating reagent N-ethylmaleimide (NEM), we have attempted to establish structure-function relationships within SRP by assembling particles in which a single protein is modified. Alkylation of the 68/72 kd protein of SRP yields a particle that arrests elongation but fails to promote translocation and no longer interacts with SRP receptor. Alkylation of the 54 kd protein yields a particle that fails to recognize signal sequences. This approach has allowed us to map activities to specific protein domains on SRP, and should be generally useful for analyzing other ribonucleoproteins.

journal_name

Cell

journal_title

Cell

authors

Siegel V,Walter P

doi

10.1016/0092-8674(88)90529-6

subject

Has Abstract

pub_date

1988-01-15 00:00:00

pages

39-49

issue

1

eissn

0092-8674

issn

1097-4172

pii

0092-8674(88)90529-6

journal_volume

52

pub_type

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